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Discovering Antioxidant Molecules in the Archaea Domain: Peroxiredoxin Bcp1 from Sulfolobus solfataricus Protects H9c2 Cardiomyoblasts from Oxidative Stress

Peroxiredoxins (Prxs) are ubiquitous thiol peroxidases that are involved in the reduction of peroxides. It has been reported that prokaryotic Prxs generally show greater structural robustness than their eukaryotic counterparts, making them less prone to inactivation by overoxidation. This difference...

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Autores principales: Sarcinelli, Carmen, Fiorentino, Gabriella, Pizzo, Elio, Bartolucci, Simonetta, Limauro, Danila
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5056240/
https://www.ncbi.nlm.nih.gov/pubmed/27752237
http://dx.doi.org/10.1155/2016/7424870
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author Sarcinelli, Carmen
Fiorentino, Gabriella
Pizzo, Elio
Bartolucci, Simonetta
Limauro, Danila
author_facet Sarcinelli, Carmen
Fiorentino, Gabriella
Pizzo, Elio
Bartolucci, Simonetta
Limauro, Danila
author_sort Sarcinelli, Carmen
collection PubMed
description Peroxiredoxins (Prxs) are ubiquitous thiol peroxidases that are involved in the reduction of peroxides. It has been reported that prokaryotic Prxs generally show greater structural robustness than their eukaryotic counterparts, making them less prone to inactivation by overoxidation. This difference has inspired the search for new antioxidants from prokaryotic sources that can be used as possible therapeutic biodrugs. Bacterioferritin comigratory proteins (Bcps) of the hyperthermophilic archaeon Sulfolobus solfataricus that belong to the Prx family have recently been characterized. One of these proteins, Bcp1, was chosen to determine its antioxidant effects in H9c2 rat cardiomyoblast cells. Bcp1 activity was measured in vitro under physiological temperature and pH conditions that are typical of mammalian cells; the yeast thioredoxin reductase (yTrxR)/thioredoxin (yTrx) reducing system was used to evaluate enzyme activity. A TAT-Bcp1 fusion protein was constructed to allow its internalization and verify the effect of Bcp1 on H9c2 rat cardiomyoblasts subjected to oxidative stress. The results reveal that TAT-Bcp1 is not cytotoxic and inhibits H(2)O(2)-induced apoptosis in H9c2 cells by reducing the H(2)O(2) content inside these cells.
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spelling pubmed-50562402016-10-17 Discovering Antioxidant Molecules in the Archaea Domain: Peroxiredoxin Bcp1 from Sulfolobus solfataricus Protects H9c2 Cardiomyoblasts from Oxidative Stress Sarcinelli, Carmen Fiorentino, Gabriella Pizzo, Elio Bartolucci, Simonetta Limauro, Danila Archaea Research Article Peroxiredoxins (Prxs) are ubiquitous thiol peroxidases that are involved in the reduction of peroxides. It has been reported that prokaryotic Prxs generally show greater structural robustness than their eukaryotic counterparts, making them less prone to inactivation by overoxidation. This difference has inspired the search for new antioxidants from prokaryotic sources that can be used as possible therapeutic biodrugs. Bacterioferritin comigratory proteins (Bcps) of the hyperthermophilic archaeon Sulfolobus solfataricus that belong to the Prx family have recently been characterized. One of these proteins, Bcp1, was chosen to determine its antioxidant effects in H9c2 rat cardiomyoblast cells. Bcp1 activity was measured in vitro under physiological temperature and pH conditions that are typical of mammalian cells; the yeast thioredoxin reductase (yTrxR)/thioredoxin (yTrx) reducing system was used to evaluate enzyme activity. A TAT-Bcp1 fusion protein was constructed to allow its internalization and verify the effect of Bcp1 on H9c2 rat cardiomyoblasts subjected to oxidative stress. The results reveal that TAT-Bcp1 is not cytotoxic and inhibits H(2)O(2)-induced apoptosis in H9c2 cells by reducing the H(2)O(2) content inside these cells. Hindawi Publishing Corporation 2016-09-26 /pmc/articles/PMC5056240/ /pubmed/27752237 http://dx.doi.org/10.1155/2016/7424870 Text en Copyright © 2016 Carmen Sarcinelli et al. https://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Sarcinelli, Carmen
Fiorentino, Gabriella
Pizzo, Elio
Bartolucci, Simonetta
Limauro, Danila
Discovering Antioxidant Molecules in the Archaea Domain: Peroxiredoxin Bcp1 from Sulfolobus solfataricus Protects H9c2 Cardiomyoblasts from Oxidative Stress
title Discovering Antioxidant Molecules in the Archaea Domain: Peroxiredoxin Bcp1 from Sulfolobus solfataricus Protects H9c2 Cardiomyoblasts from Oxidative Stress
title_full Discovering Antioxidant Molecules in the Archaea Domain: Peroxiredoxin Bcp1 from Sulfolobus solfataricus Protects H9c2 Cardiomyoblasts from Oxidative Stress
title_fullStr Discovering Antioxidant Molecules in the Archaea Domain: Peroxiredoxin Bcp1 from Sulfolobus solfataricus Protects H9c2 Cardiomyoblasts from Oxidative Stress
title_full_unstemmed Discovering Antioxidant Molecules in the Archaea Domain: Peroxiredoxin Bcp1 from Sulfolobus solfataricus Protects H9c2 Cardiomyoblasts from Oxidative Stress
title_short Discovering Antioxidant Molecules in the Archaea Domain: Peroxiredoxin Bcp1 from Sulfolobus solfataricus Protects H9c2 Cardiomyoblasts from Oxidative Stress
title_sort discovering antioxidant molecules in the archaea domain: peroxiredoxin bcp1 from sulfolobus solfataricus protects h9c2 cardiomyoblasts from oxidative stress
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5056240/
https://www.ncbi.nlm.nih.gov/pubmed/27752237
http://dx.doi.org/10.1155/2016/7424870
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